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Sodium in PDB 1ge2: Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions

Enzymatic activity of Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions

All present enzymatic activity of Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions, PDB code: 1ge2 was solved by K.Takano, Y.Yamagata, K.Yutani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.310, 61.620, 33.510, 90.00, 90.00, 90.00
R / Rfree (%) 16 / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions (pdb code 1ge2). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions, PDB code: 1ge2:

Sodium binding site 1 out of 1 in 1ge2

Go back to Sodium Binding Sites List in 1ge2
Sodium binding site 1 out of 1 in the Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Mutant Human Lysozyme Substituted at Left-Handed Helical Positions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na601

b:13.4
occ:1.00
O A:HOH252 2.3 28.0 1.0
O A:HOH203 2.5 19.4 1.0
O A:HOH146 4.5 14.1 1.0
O A:HOH164 4.9 9.9 1.0

Reference:

K.Takano, Y.Yamagata, K.Yutani. Role of Non-Glycine Residues in Left-Handed Helical Conformation For the Conformational Stability of Human Lysozyme Proteins V. 44 233 2001.
ISSN: ISSN 0887-3585
PubMed: 11455596
DOI: 10.1002/PROT.1088
Page generated: Tue Dec 15 05:24:24 2020

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